CNGA2_HUMAN
ID CNGA2_HUMAN Reviewed; 664 AA.
AC Q16280; A0AVD0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cyclic nucleotide-gated olfactory channel;
DE AltName: Full=Cyclic nucleotide-gated cation channel 2;
DE AltName: Full=Cyclic nucleotide-gated channel alpha-2;
DE Short=CNG channel alpha-2;
DE Short=CNG-2;
DE Short=CNG2;
GN Name=CNGA2; Synonyms=CNCA, CNCA1, CNCG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 292-552.
RX PubMed=7532814; DOI=10.1016/0028-3908(94)90027-2;
RA Distler M., Biel M., Flockerzi V., Hofmann F.;
RT "Expression of cyclic nucleotide-gated cation channels in non-sensory
RT tissues and cells.";
RL Neuropharmacology 33:1275-1282(1994).
RN [3]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-97 AND GLN-399.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Odorant signal transduction is probably mediated by a G-
CC protein coupled cascade using cAMP as second messenger. The olfactory
CC channel can be shown to be activated by cyclic nucleotides which leads
CC to a depolarization of olfactory sensory neurons.
CC -!- SUBUNIT: Heterotetramer composed of two subunits of CNGA2, one of CNGA4
CC and one of CNGB1b. The complex forms the cyclic nucleotide-gated (CNG)
CC channel of olfactory sensory neurons (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The C-terminal coiled-coil domain mediates trimerization of
CC CNGA subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGA2 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC126302; AAI26303.1; -; mRNA.
DR EMBL; BC126304; AAI26305.1; -; mRNA.
DR EMBL; S76067; AAD14207.1; -; Genomic_DNA.
DR CCDS; CCDS14701.1; -.
DR PIR; I78559; I78559.
DR RefSeq; NP_005131.1; NM_005140.1.
DR AlphaFoldDB; Q16280; -.
DR SMR; Q16280; -.
DR STRING; 9606.ENSP00000328478; -.
DR DrugCentral; Q16280; -.
DR GuidetoPHARMACOLOGY; 395; -.
DR GlyGen; Q16280; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q16280; -.
DR PhosphoSitePlus; Q16280; -.
DR BioMuta; CNGA2; -.
DR DMDM; 119370323; -.
DR MassIVE; Q16280; -.
DR PaxDb; Q16280; -.
DR PeptideAtlas; Q16280; -.
DR PRIDE; Q16280; -.
DR ProteomicsDB; 60847; -.
DR Antibodypedia; 17043; 262 antibodies from 30 providers.
DR DNASU; 1260; -.
DR Ensembl; ENST00000329903.5; ENSP00000328478.4; ENSG00000183862.6.
DR GeneID; 1260; -.
DR KEGG; hsa:1260; -.
DR MANE-Select; ENST00000329903.5; ENSP00000328478.4; NM_005140.3; NP_005131.1.
DR UCSC; uc065bqd.1; human.
DR CTD; 1260; -.
DR DisGeNET; 1260; -.
DR GeneCards; CNGA2; -.
DR HGNC; HGNC:2149; CNGA2.
DR HPA; ENSG00000183862; Not detected.
DR MalaCards; CNGA2; -.
DR MIM; 300338; gene.
DR neXtProt; NX_Q16280; -.
DR OpenTargets; ENSG00000183862; -.
DR Orphanet; 88620; Isolated congenital anosmia.
DR PharmGKB; PA26659; -.
DR VEuPathDB; HostDB:ENSG00000183862; -.
DR eggNOG; KOG0500; Eukaryota.
DR GeneTree; ENSGT00940000155374; -.
DR HOGENOM; CLU_005746_12_0_1; -.
DR InParanoid; Q16280; -.
DR OMA; FPIIRQA; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q16280; -.
DR TreeFam; TF319048; -.
DR PathwayCommons; Q16280; -.
DR Reactome; R-HSA-381753; Olfactory Signaling Pathway.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; Q16280; -.
DR BioGRID-ORCS; 1260; 11 hits in 686 CRISPR screens.
DR GeneWiki; Cyclic_nucleotide-gated_channel_alpha_2; -.
DR GenomeRNAi; 1260; -.
DR Pharos; Q16280; Tchem.
DR PRO; PR:Q16280; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q16280; protein.
DR Bgee; ENSG00000183862; Expressed in testis and 1 other tissue.
DR GO; GO:0060170; C:ciliary membrane; ISS:ARUK-UCL.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IBA:GO_Central.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR032406; CLZ_dom.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF16526; CLZ; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding; cAMP; cAMP-binding; Coiled coil; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Nucleotide-binding; Olfaction; Reference proteome; Sensory transduction;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..664
FT /note="Cyclic nucleotide-gated olfactory channel"
FT /id="PRO_0000219312"
FT TOPO_DOM 1..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..453
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 597..640
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454..577
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 97
FT /note="R -> H (in a breast cancer sample; somatic mutation;
FT dbSNP:rs561786347)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036603"
FT VARIANT 118
FT /note="D -> H (in dbSNP:rs6627455)"
FT /id="VAR_048748"
FT VARIANT 139
FT /note="W -> L (in dbSNP:rs35350051)"
FT /id="VAR_061107"
FT VARIANT 399
FT /note="R -> Q (in a breast cancer sample; somatic mutation;
FT dbSNP:rs150539917)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036604"
FT VARIANT 663
FT /note="E -> K (in dbSNP:rs714147)"
FT /id="VAR_048749"
SQ SEQUENCE 664 AA; 76048 MW; E8FB934468429CE5 CRC64;
MTEKTNGVKS SPANNHNHHA PPAIKANGKD DHRTSSRPHS AADDDTSSEL QRLADVDAPQ
QGRSGFRRIV RLVGIIREWA NKNFREEEPR PDSFLERFRG PELQTVTTQE GDGKGDKDGE
DKGTKKKFEL FVLDPAGDWY YCWLFVIAMP VLYNWCLLVA RACFSDLQKG YYLVWLVLDY
VSDVVYIADL FIRLRTGFLE QGLLVKDTKK LRDNYIHTLQ FKLDVASIIP TDLIYFAVDI
HSPEVRFNRL LHFARMFEFF DRTETRTNYP NIFRISNLVL YILVIIHWNA CIYYAISKSI
GFGVDTWVYP NITDPEYGYL AREYIYCLYW STLTLTTIGE TPPPVKDEEY LFVIFDFLIG
VLIFATIVGN VGSMISNMNA TRAEFQAKID AVKHYMQFRK VSKGMEAKVI RWFDYLWTNK
KTVDEREILK NLPAKLRAEI AINVHLSTLK KVRIFHDCEA GLLVELVLKL RPQVFSPGDY
ICRKGDIGKE MYIIKEGKLA VVADDGVTQY ALLSAGSCFG EISILNIKGS KMGNRRTANI
RSLGYSDLFC LSKDDLMEAV TEYPDAKKVL EERGREILMK EGLLDENEVA TSMEVDVQEK
LGQLETNMET LYTRFGRLLA EYTGAQQKLK QRITVLETKM KQNNEDDYLS DGMNSPELAA
ADEP
